Effects of Hydrophobic Amino Acid Substitutions on Antimicrobial Peptide Behavior.

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Antibacterial Activity and Mechanism of Action of Bovine Lactoferricin Derivatives with Symmetrical Amino Acid Sequences

P2860

Q59138325-55634707-2F73-4974-8CF8-BB96570CC1AC

P2860

Effects of Hydrophobic Amino Acid Substitutions on Antimicrobial Peptide Behavior.

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http://www.wikidata.org/entity/Q47441212

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2017 nî lūn-bûn

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2017年の論文

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2017年学术文章

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2017年学术文章

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2017年学术文章

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Effects of Hydrophobic Amino Acid Substitutions on Antimicrobial Peptide Behavior.

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Effects of Hydrophobic Amino Acid Substitutions on Antimicrobial Peptide Behavior.

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Effects of Hydrophobic Amino Acid Substitutions on Antimicrobial Peptide Behavior.

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Effects of Hydrophobic Amino Acid Substitutions on Antimicrobial Peptide Behavior.

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Effects of Hydrophobic Amino Acid Substitutions on Antimicrobial Peptide Behavior.

@en

Effects of Hydrophobic Amino Acid Substitutions on Antimicrobial Peptide Behavior.

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P1476

Effects of Hydrophobic Amino Acid Substitutions on Antimicrobial Peptide Behavior.

@en

P2093

Christina L Chrom

http://www.w3.org/2001/XMLSchema#string

Gregory A Caputo

http://www.w3.org/2001/XMLSchema#string

Karlee D Henderson

http://www.w3.org/2001/XMLSchema#string

Kimberly D Saint Jean

http://www.w3.org/2001/XMLSchema#string

Lindsay M Renn

http://www.w3.org/2001/XMLSchema#string

Louisa E Abiuso

http://www.w3.org/2001/XMLSchema#string

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A simple method for displaying the hydropathic character of a protein

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Antibiotic development challenges: the various mechanisms of action of antimicrobial peptides and of bacterial resistance

Functional characterization of a melittin analog containing a non-natural tryptophan analog

Cumulative effects of amino acid substitutions and hydrophobic mismatch upon the transmembrane stability and conformation of hydrophobic alpha-helices

Defensins: antimicrobial peptides of innate immunity

Analysis of membrane and surface protein sequences with the hydrophobic moment plot

Combining hydrophobicity and helicity: a novel approach to membrane protein structure prediction.

Hydrogen-bond energetics drive helix formation in membrane interfaces.

A PhoP-regulated outer membrane protease of Salmonella enterica serovar typhimurium promotes resistance to alpha-helical antimicrobial peptides.

P2888

s12602-017-9345-z

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scholarly article

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10.1007/S12602-017-9345-Z

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P577

2017-11-04T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

29103131

http://www.w3.org/2001/XMLSchema#string

P921

hydrophobicity

Effects of Hydrophobic Amino Acid Substitutions on Antimicrobial Peptide Behavior.

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P2860

P2860

Effects of Hydrophobic Amino Acid Substitutions on Antimicrobial Peptide Behavior.

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P1433

P1476

P2093

P2860

P2888

P31

P356

P577

P698

P921

P356

P1433

P1476

P2093

P2860

P2888

P31

P356

P577

P698

P921